The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Listeria monocytogenes transiently alters mitochondrial dynamics during infection
Open accessAbstract
Mitochondria are essential and highly dynamic organelles, constantly undergoing fusion and fission. We analyzed mitochondrial dynamics during infection with the human bacterial pathogen Listeria monocytogenes and show that this infection profoundly alters mitochondrial dynamics by causing transient mitochondrial network fragmentation. Mitochondrial fragmentation is specific to pathogenic Listeria monocytogenes , and it is not observed with the nonpathogenic Listeria innocua species or several other intracellular pathogens. Strikingly, the efficiency of Listeria infection is affected in cells where either mitochondrial fusion or fission has been altered by siRNA treatment, highlighting the relevance of mitochondrial dynamics for Listeria infection. We identified the secreted pore-forming toxin listeriolysin O as the bacterial factor mainly responsible for mitochondrial network disruption and mitochondrial function modulation. Together, our results suggest that the transient shutdown of mitochondrial function and dynamics represents a strategy used by Listeria at the onset of infection to interfere with cellular physiology.
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The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
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Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
Control of mitochondrial morphology by a human mitofusin
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“Key players in the fusion process include the outer mitochondrial membrane GTPases mitofusin 1 and 2 (Mfn1/2) (8, 9), and the inner membrane GTPase optic atrophy 1 (Opa1) (10, 11), but the molecular details of the fusion mechanism remain obscure (12, 13).”
BackgroundHumphries, J. D., Byron, A., Bass, M. D., Craig, S. E., Pinney, J. W., Knight, D., & Humphries, M. J. (2009) · Science Signaling · doi:10.1126/scisignal.2000396 · Cited by 404
Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway
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Mitofusin 2 Inhibits Mitochondrial Antiviral Signaling
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The ubiquitin ligase parkin mediates resistance to intracellular pathogens
Manzanillo, P. S., Ayres, J. S., Watson, R. O., Collins, A. C., Souza, G., Rae, C. S., Schneider, D. S., Nakamura, K., Shiloh, M. U., & Cox, J. S. (2013) · Nature · doi:10.1038/nature12566 · Cited by 588
Molecular mechanisms of mitochondrial dynamics
Tábara, L.-C., Segawa, M., & Prudent, J. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 406
Mitochondria as a Cellular Hub in Infection and Inflammation
Andrieux, P., Chevillard, C., Cunha-Neto, E., & Nunes, J. P. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111338 · Cited by 346
Listeriolysin O: the Swiss army knife of Listeria
Hamon, M. A., Ribet, D., Stavru, F., & Cossart, P. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.04.006 · Cited by 295
Self-citation
Metadata
- Authors
- Stavru, F., Bouillaud, F., Sartori, A., Ricquier, D., & Cossart, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-02-14
- Volume
- 108
- Issue
- 9
- Pages
- 3612-3617
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2027426716
- Cited by
- 248
- References
- 10
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- green
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